RF1_STRU0
ID RF1_STRU0 Reviewed; 359 AA.
AC B9DS45;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=SUB0871;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
CC -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC translation in response to the peptide chain termination codons UAG and
CC UAA. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR EMBL; AM946015; CAR41933.1; -; Genomic_DNA.
DR RefSeq; WP_012658373.1; NC_012004.1.
DR AlphaFoldDB; B9DS45; -.
DR SMR; B9DS45; -.
DR STRING; 218495.SUB0871; -.
DR PRIDE; B9DS45; -.
DR EnsemblBacteria; CAR41933; CAR41933; SUB0871.
DR KEGG; sub:SUB0871; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_9; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR Proteomes; UP000000449; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00093; Rel_fac_1; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004373; RF-1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR TIGRFAMs; TIGR00019; prfA; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT CHAIN 1..359
FT /note="Peptide chain release factor 1"
FT /id="PRO_1000193511"
FT REGION 288..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 359 AA; 40740 MW; 088C48783082EF3F CRC64;
MNIYDQLQSL EDRYEELGEL LSDPEVVSDT KRFMELSKEE ANTRETVATY RQYKDIIQSI
SDAEEMIKES GGDPEIEEMA KEELKESKVA KEDYEEKLKI LLLPKDPNDD KNIILEIRGA
AGGDEAALFA GDLLDMYQRF AESQGWRFEV MEASYNGVGG IKEVVAMVSG QSVYSKLKYE
SGAHRVQRVP VTESQGRVHT STATVLVMPE IEDVEYDIDP KDLRIDIYHA SGAGGQNVNK
VATAVRIVHL PTNIKVEMQE ERTQQKNRDK AMKIIRARVA DHFAQIAQDE QDAERKSTIG
TGDRSERIRT YNFPQNRVTD HRIGLTLQKL DTILSGKMDE VIDALVMYDQ TQKLETLNQ